Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:4.1.1.17 (ornithine decarboxylase)
 6,351 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Diamine oxidase and ornithine decarboxylase activities are shown to have a parallel distribution across rat small intestine mucosa; levels of both enzyme activities are sharply higher in mature cells in the villus tip region than in proliferating cells in the crypt areas. Histidine decarboxylase levels were not measurable in the same cell preparations and aromatic-L-amino-acid decarboxylase activity was distributed in an opposite pattern to diamine oxidase and ornithine decarboxylase. The results suggest that intestinal diamine oxidase could be involved with polyamine metabolism. The new findings for ornithine decarboxylase suggest an in vivo role for polyamines in non-proliferative cells; rat small intestinal mucosa may be an excellent model for investigating the function of polyamines in regenerating cells.
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PMID:Association of diamine oxidase and ornithine decarboxylase with maturing cells in rapidly proliferating epithelium. 9 70

1. Histidine decarboxylase and ornithine decarboxylase activities were determined in mouse kidney and liver during post-natal development. 2. The content of histamine, putrescine, spermidine and spermine was examined in kidney and liver and in the urine of adult male and female mice. 3. Histamine formation by the kidney was high in both sexes when determined a few days after birth but decreased during weaning. Thereafter, a distinct sex difference was established in that in the female kidney the level of histidine decarboxylase rose several-fold during adolescence while in the male the level was still further reduced. 4. Putrescine formation by mouse kidney was low in both sexes up to three weeks of age whereafter the amine formation in the male increased conspicuously whereas that of the female kidney remained low. 5. The observed sex differences in tissue enzyme activities were reflected in concomitant differences in the amount of the diamines excreted in the urine. 6. No correlation was found between the actual enzyme levels and the assayed tissue content of histamine, putrescine, spermidine and spermine. 7. Following gonadectomy, the activities of both decarboxylases were significantly altered. Ornithine decarboxylase activity of male kidney and histidine decarboxylase activity of female kidney were strikingly reduced. 8. In the mouse liver, the two decarboxylases displayed no changes comparable with that of the kidney during development.
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PMID:Biosynthesis of histamine and putrescine in mice during post-natal development and its hormone dependence. 114 82

1. The urinary excretion of putrescine has been determined in female mice before and during repeated injections of testosterone.2. Testosterone administration effected a striking increase in the excretion of free putrescine.3. Ornithine decarboxylase (L-ornithine carboxy-lyase; E.C. 4.1.1.17) and histidine decarboxylase (L-histidine carboxy-lyase; E.C. 4.1.1.22) activities of mouse kidney and liver were examined. In the kidney, following testosterone administration, ornithine decarboxylase activity was found to be substantially elevated, whereas that of histidine decarboxylase was depressed. In the liver, by contrast, the activity levels of these enzymes were not significantly altered by testosterone treatment.4. The possibility of a functional interrelation between putrescine and histamine, via the two enzyme activities investigated, is discussed.
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PMID:Alterations in the activities of ornithine and histidine decarboxylases provoked by testosterone in mice. 472 83

1. The activities of histidine and ornithine decarboxylases as well as the histamine content of the developing chick embryo were studied.2. Histidine decarboxylase (L-histidine carboxy-lyase; E.C. 4.1.1.22) activity was fairly low with a tendency to increase at later stages of development. This enzyme was preferentially present in the supernatant fraction of the tissue homogenate. alpha-Methyl-histidine, but not alpha-methyl-DOPA, inhibited its activity.3. The histamine content per gramme of embryo was low with a tendency to increase with the age of the embryo.4. Ornithine decarboxylase (L-ornithine carboxy-lyase; E.C. 4.1.1.17) activity was high at the beginning of the stages of development investigated, but later there was a steep fall in activity. A noticeable feature was that while the activity in the residual fraction of the homogenate remained almost constant during development, the activity in the supernatant fraction was high in the early stages, then fell rapidly to nearly zero at later stages.
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PMID:Decarboxylases of histidine and ornithine in chick embryo. 557 79

Histidine decarboxylase (HisDCase, EC 4.1.1.22) activity in mouse skin increased by a factor of more than 10 after a single application of phorbol 12-myristate 13-acetate. The cell type that was responsible for the increase in HisDCase activity was examined by using (WB X C57BL/6)F1-W/Wv mice, which are genetically deficient in tissue mast cells. In contrast to a report that increase of ornithine decarboxylase (EC 4.1.1.17) activity occurs in the epidermis [O'Brien, T. G., Simisiman, R. C. & Boutwell, R. K. (1975) Cancer Res. 35, 2426-2433], the HisDCase activity was found to increase in the dermis. Although most of the histamine in the dermis was present in mast cells, the increase in HisDCase activity in the skin in W/Wv mice was comparable with that in congeneic +/+ mice. This increase of HisDCase activity in the skin of W/Wv mice was abolished by prior x-ray irradiation (800 rads; 1 rad = 0.01 gray) but was restored by subsequent bone marrow transplantation. Because mice, in general, are known to lack basophilic leukocytes, the present results suggest the existence of histamine-producing cells without basophilic granules that are derived from the bone marrow.
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PMID:Increase in histidine decarboxylase activity in skin of genetically mast-cell-deficient W/Wv mice after application of phorbol 12-myristate 13-acetate: evidence for the presence of histamine-producing cells without basophilic granules. 696 Mar 52

L-Ornithine decarboxylase was purified to apparent homogeneity from the kidneys of testosterone-treated mice. Antibodies to ornithine decarboxylase were raised in a rabbit using the purified enzyme. Ouchterlony double diffusion technique revealed a single precipitin line between the antiserum and purified mouse kidney ornithine decarboxylase. The antibodies inhibited ornithine decarboxylase from various tissues of mice and rats to the same extent, indicating a close immunological relationship. S-Adenosyl-L-methionine decarboxylase and L-histidine decarboxylase from mouse kidney as well as ornithine decarboxylase from Escherichia coli were unaffected by the antibodies.
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PMID:Antibodies to ornithine decarboxylase. Immunochemical cross-reactivity. 716 4

We previously demonstrated that both histamine synthesis (histidine decarboxylase activity) and polyamine synthesis (ornithine decarboxylase activity) increased in the rat intestinal mucosa after ischemia-reperfusion, whereas the relationship between these two factors remains unclear. To elucidate this relationship, we performed the present study. The superior mesenteric artery was occluded for 15 min followed by reperfusion. After ischemia-reperfusion, histidine decarboxylase activity and ornithine decarboxylase activity in the rat jejunal mucosa were measured in a time-dependent manner. Histidine decarboxylase activity increased 1 hr after ischemia-reperfusion, although ornithine decarboxylase activity did not; however, its activity did increase 6 hr after. The increase of ornithine decarboxylase activity was attenuated when the increase of histamine synthesis was suppressed by the inhibition of histidine decarboxylase activity caused by pretreatment with alpha-fluoromethylhistidine, a suicide inhibitor of histidine decarboxylase. Pretreatment with H1-receptor antagonist attenuated the increase of ornithine decarboxylase activity after ischemia-reperfusion. These results indicate that the newly synthesized histamine, as indicated by an increase of histidine decarboxylase activity, increases ornithine decarboxylase activity after ischemia-reperfusion of the rat intestinal mucosa.
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PMID:Newly synthesized histamine accelerates ornithine decarboxylase activity in rat intestinal mucosa after ischemia-reperfusion. 772 Apr 59

Control of enzymatic function by peptide hormones can occur at a number of different levels and can involve diverse pathways that regulate cleavage, intracellular trafficking, and protein degradation. Gastrin is a peptide hormone that binds to the cholecystokinin B-gastrin receptor and regulates the activity of L-histidine decarboxylase (HDC), the enzyme that produces histamine. Here we show that gastrin can increase the steady-state levels of at least six HDC isoforms without affecting HDC mRNA levels. Pulse-chase experiments indicated that HDC isoforms are rapidly degraded and that gastrin-dependent increases are due to enhanced isoform stability. Deletion analysis identified two PEST domains (PEST1 and PEST2) and an intracellular targeting domain (ER2) which regulate HDC protein expression levels. Experiments with PEST domain fusion proteins demonstrated that PEST1 and PEST2 are strong and portable degradation-promoting elements which are positively regulated by both gastrin stimulation and proteasome inhibition. A chimeric protein containing the PEST domain of ornithine decarboxylase was similarly affected, indicating that gastrin can regulate the stability of other PEST domain-containing proteins and does so independently of antizyme/antizyme inhibitor regulation. At the same time, endoplasmic reticulum localization of a fluorescent chimera containing the ER2 domain of HDC was unaltered by gastrin stimulation. We conclude that gastrin stabilization of HDC isoforms is dependent upon two transferable and sequentially unrelated PEST domains that regulate degradation. These experiments revealed a novel regulatory mechanism by which a peptide hormone such as gastrin can disrupt the degradation function of multiple PEST-domain-containing proteins.
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PMID:Amino- and carboxy-terminal PEST domains mediate gastrin stabilization of rat L-histidine decarboxylase isoforms. 1084 18

Histamine system is suggested to have a role in mammary gland growth regulation, differentiation and functioning during pregnancy and lactation. Histidine decarboxylase activity undergoes significant changes during pregnancy and lactation. Pregnancy associated elevation of HDC activity and mRNA transcript in mouse mammary gland was successfully affected by enzyme antisense oligonucleotides treatment. The enzyme activity of resting mammae was unaffected as it lacked inducible pool of HDC. The short-term mammary histamine shortage evoked influenced the mRNA expression of histamine receptors (H1 and H2) and ornithine decarboxylase during pregnancy. There were essentially no morphological changes in the mammary gland upon the treatment, however, adipocytes neighbouring alveolar structures were more pronounced. These findings further substantiate the role of histamine in mammary gland physiology and emphasise presence of common motifs of biogenic amines and polyamine metabolism as well as mutual interferences implicating observed "cross-talk" phenomenon.
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PMID:Mammary histidine decarboxylase vulnerability to enzyme antisense oligonucleotides: histamine and polyamine systems cross-talk. 1529 Mar 35